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Identification of Fructose-1,6-bisphosphate aldolase cytosolic class I as an NMH7 MADS domain associated protein

2008; Elsevier BV; Volume: 376; Issue: 4 Linguagem: Inglês

10.1016/j.bbrc.2008.09.064

1090-2104

Julio Paéz-Valencia, Pedro Valencia‐Mayoral, Concepción Sánchez‐Gómez, Alejandra Contreras‐Ramos, Ismael Hernández-Lucas, Eleazar Martínez‐Barajas, Alicia Gamboa‐deBuen,

Plant nutrient uptake and metabolism

We are interested in identifying proteins that interact with the MADS domain protein NMH7 of Medicago sativa. We use an affinity column with a synthetic peptide derived from the MADS domain of NMH7 which has been reported to mediate protein–protein interaction with non-MADS domain interacting proteins. We identified ∼40 and ∼80 kDa specifically bound proteins as the monomeric and dimeric forms of Fructose-1,6-bisphosphate aldolase cytosolic class I. NiNTA pull down assays revealed that K- and C-terminus regions of NMH7 are not required for the interaction with aldolase. Aldolase enzymatic activity is not required for the interaction with NMH7. NMH7 and aldolase were coimmunoprecipitated from non-inoculated seed and seedlings extracts. Colocalization studies using confocal microscopy showed that aldolase and NMH7 are localized in the cytoplasm and the nucleus of the cortical cells. These data together show that M. sativa aldolase is a novel MADS domain binding protein, and suggest a broader functional repertory for this enzyme, as has been proposed for other glycolytic enzymes.